Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The Identification of Host Proteins That Interact with Non-Structural Proteins-1α and -1β of Porcine Reproductive and Respiratory Syndrome Virus-1

16 Dec 2023

Abstract excerpt

Porcine reproductive and respiratory syndrome viruses (PRRSV-1 and -2) are the causative agents of one of the most important infectious diseases affecting the global pig industry. Previous studies, largely focused on PRRSV-2, have shown that non-structural protein-1α (NSP1α) and NSP1β modulate host cell responses; however, the underlying molecular mechanisms remain to be fully elucidated. Therefore, we aimed to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Animal Virus Infections Studies
Share to Viral gastroenteritis research and epidemiology
Share to Virus-based gene therapy research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 38140685
DOI: 10.3390/v15122445

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Identification of Host Proteins That Interact with Non-Structural Proteins-1α and -1β of Porcine Reproductive and Respiratory Syndrome Virus-1PMID 38140685Read ↗

THAP11-mediated K48- and K63-linked ubiquitination is essential for the degradation of porcine reproductive and respiratory syndrome virus nonstructural protein 1βSemantic proximity Read ↗

THAP11-mediated K48- and K63-linked ubiquitination is essential for the degradation of porcine reproductive and respiratory syndrome virus nonstructural protein 1βSemantic proximity Read ↗

Research Progress in Porcine Reproductive and Respiratory Syndrome Virus–Host Protein InteractionsSemantic proximity Read ↗

Exploring virus-host interactions through combined proteomic approaches identifies BANF1 as a new essential factor for African Swine Fever VirusSemantic proximity Read ↗

Cellular Poly(C) Binding Proteins 1 and 2 Interact with Porcine Reproductive and Respiratory Syndrome Virus Nonstructural Protein 1β and Support Viral ReplicationSemantic proximity Read ↗

The role of porcine reproductive and respiratory syndrome (PRRS) virus structural and non-structural proteins in virus pathogenesisSemantic proximity Read ↗

PSMB1 Inhibits the Replication of Porcine Reproductive and Respiratory Syndrome Virus by Recruiting NBR1 To Degrade Nonstructural Protein 12 by AutophagySemantic proximity Read ↗

Interaction network of African swine fever virus structural protein p30 with host proteinsSemantic proximity Read ↗

Research Progress on the NSP10 Protein of Porcine Reproductive and Respiratory Syndrome VirusSemantic proximity Read ↗

Porcine Reproductive and Respiratory Syndrome Virus (PRRSV): Pathogenesis and Interaction with the Immune SystemSemantic proximity Read ↗

Functional Landscape of African Swine Fever Virus–Host and Virus–Virus Protein InteractionsSemantic proximity Read ↗

Research Progress on the NSP9 Protein of Porcine Reproductive and Respiratory Syndrome VirusSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.